ID A0A1Y3CJD0_9GAMM Unreviewed; 398 AA.
AC A0A1Y3CJD0;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Probable peptidoglycan glycosyltransferase FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE Short=PGT {ECO:0000256|HAMAP-Rule:MF_00913};
DE EC=2.4.1.129 {ECO:0000256|HAMAP-Rule:MF_00913};
DE AltName: Full=Cell division protein FtsW {ECO:0000256|HAMAP-Rule:MF_00913};
DE AltName: Full=Cell wall polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE AltName: Full=Peptidoglycan polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
DE Short=PG polymerase {ECO:0000256|HAMAP-Rule:MF_00913};
GN Name=ftsW {ECO:0000256|HAMAP-Rule:MF_00913};
GN ORFNames=B9T28_00925 {ECO:0000313|EMBL:OTG67229.1};
OS Acinetobacter silvestris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1977882 {ECO:0000313|EMBL:OTG67229.1, ECO:0000313|Proteomes:UP000242765};
RN [1] {ECO:0000313|EMBL:OTG67229.1, ECO:0000313|Proteomes:UP000242765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4999 {ECO:0000313|EMBL:OTG67229.1,
RC ECO:0000313|Proteomes:UP000242765};
RA Nemec A., Radolfova-Krizova L.;
RT "High diversity of culturable Acinetobacter species in natural soil and
RT water ecosystems.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptidoglycan polymerase that is essential for cell division.
CC {ECO:0000256|HAMAP-Rule:MF_00913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988, ECO:0000256|HAMAP-
CC Rule:MF_00913};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|HAMAP-Rule:MF_00913}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00913}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00913}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}. Note=Localizes to the
CC division septum. {ECO:0000256|HAMAP-Rule:MF_00913}.
CC -!- SIMILARITY: Belongs to the SEDS family. FtsW subfamily.
CC {ECO:0000256|ARBA:ARBA00038053, ECO:0000256|HAMAP-Rule:MF_00913}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTG67229.1}.
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DR EMBL; NEGB01000001; OTG67229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y3CJD0; -.
DR STRING; 1977882.B9T28_00925; -.
DR OrthoDB; 9768187at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000242765; Unassembled WGS sequence.
DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-UniRule.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR HAMAP; MF_00913; PGT_FtsW_proteobact; 1.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR013437; FtsW.
DR InterPro; IPR001182; FtsW/RodA.
DR NCBIfam; TIGR02614; ftsW; 1.
DR PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR PANTHER; PTHR30474:SF2; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE FTSW-RELATED; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW Rule:MF_00913};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW Rule:MF_00913}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00913};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00913};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00913};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00913};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_00913};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00913};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00913};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00913};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00913};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00913}.
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 97..114
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 126..150
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 162..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 185..202
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 326..347
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00913"
SQ SEQUENCE 398 AA; 43681 MW; B8668917F446CAEF CRC64;
MAGLAQTTIS KINQVYDKWL PKLPAELTAR NVLIFCVIAL LCIGSVMVAS ASMPYAERMH
EAPFHYVIRH AISIVVAAAA ALFVYKISLN VWFKNTFPFW LLTIFLLLAV LLVGTEVNGS
TRWIRIGGFT LQATEVAKVM MAIFTADYVV RRAEEVRNNI KGLVRLGAVM LITVGLIIAE
PDLGATVVIA VMMLGVFFLA GAPLIQFGIA FGAILSAFVF LIVFEPYRYE RLMSFSNPWA
DPLGTGYQLS NALMAFGRGE WFGVGLGHSI QKMSYLPEAH TDFMLAILGE EFGFFGIATV
LTLSFVMLAC CIRIGHRALQ HQYLRAGYLA YGISIIFLLQ ILVNAGMNMG MLPTKGLTLP
FISYGGSSLI MCAVMISLIL KIDVTTQKAN PAREESSF
//
